112229-39-7Relevant academic research and scientific papers
Synthesis and in vitro enzyme activity of aza, oxa and thia derivatives of bacterial cell wall biosynthesis intermediates
Cox,Wang
, p. 2022 - 2034 (2007/10/03)
Mechanism based inhibitors of diaminopimelate aminotransferase (DAP-AT) were designed using knowledge of its substrate specificity and mechanism. Synthesis of thiolester and amide substrate analogues was achieved prior to in vitro inhibition studies, but ester analogues proved too unstable to isolate. Thia substrate analogues showed no inhibitory properties, but the aza substrate analogue 12a showed reversible inhibition vs. DAP-AT and time dependent inhibition in the absence of the natural substrate 4. Substrate analogue 12a is thefirst example of an amide inhibitor of PLP dependent enzymes. Antibiotic properties of 12a were also briefly assessed.
Hydroboration of vinylglycine and allylglycine as a route to boron- derivatives of α-amino acids
Denniel, Valerie,Bauchat, Patrick,Danion, Daniel,Danion-Bougot, Renee
, p. 5111 - 5114 (2007/10/03)
The hydroboration of protected vinylglycine and allylglycine with dicyclohexyl- or diisopinocampheylborane occurs chimio- and regioselectively with attachment of boron to the less substituted end of the carbon-carbon double bond. Homoserine or δ-hydroxynorvaline are readily obtained by H2O2/CH3CO2Na oxidation of dicyclohexylborane derivatives and 2-amino-4- boronobutanoic acid or 2-amino-5-boronopentanoic acid by reaction of diisopinocampheylborane derivatives with excess of ethanal and deprotection.
